Issue 83, 2014
From the journal:

Chemical Communications

Co(ii)/Co(i) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model†

Takashi Hayashi,*a   Yoshitsugu Morita,a   Eiichi Mizohata,a   Koji Oohora,a   Jun Ohbayashi,a   Tsuyoshi Inouea  and  Yoshio Hisaedab  

* Corresponding authors

a Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita 565-0871, Japan
E-mail: thayashi@chem.eng.osaka-u.ac.jp

b Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka 819-0395, Japan

Abstract

A conjugate between apomyoglobin and cobalt tetradehydrocorrin was prepared to replicate the coordination behavior of cob(I)alamin in methionine synthase. X-ray crystallography reveals that the tetra-coordinated Co(I) species is formed through the cleavage of the axial Co–His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket.

Graphical abstract: Co(ii)/Co(i) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model

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Article information

DOI
https://doi.org/10.1039/C4CC05448B
Article type
Communication
Submitted
15 Jul 2014
Accepted
27 Aug 2014
First published
28 Aug 2014
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2014,50, 12560-12563

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Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model

T. Hayashi, Y. Morita, E. Mizohata, K. Oohora, J. Ohbayashi, T. Inoue and Y. Hisaeda, Chem. Commun., 2014, 50, 12560 DOI: 10.1039/C4CC05448B

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